ID G8PBA2_PEDCP Unreviewed; 548 AA.
AC G8PBA2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Trehalose-6-phosphate hydrolase {ECO:0000313|EMBL:AEV95891.1};
GN Name=treC {ECO:0000313|EMBL:AEV95891.1};
GN OrderedLocusNames=PECL_1674 {ECO:0000313|EMBL:AEV95891.1};
OS Pediococcus claussenii (strain ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC
OS 3811 / P06).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=701521 {ECO:0000313|EMBL:AEV95891.1, ECO:0000313|Proteomes:UP000005444};
RN [1] {ECO:0000313|Proteomes:UP000005444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC {ECO:0000313|Proteomes:UP000005444};
RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA Kusalik A., Ziola B.;
RT "Genome and plasmid sequences for the beer-spoilage organism Pediococcus
RT claussenii ATCC BAA-344T.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV95891.1, ECO:0000313|Proteomes:UP000005444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-344 / DSM 14800 / JCM 18046 / KCTC 3811 / P06
RC {ECO:0000313|Proteomes:UP000005444};
RX PubMed=22328764; DOI=10.1128/JB.06759-11;
RA Pittet V., Abegunde T., Marfleet T., Haakensen M., Morrow K.,
RA Jayaprakash T., Schroeder K., Trost B., Byrns S., Bergsveinson J.,
RA Kusalik A., Ziola B.;
RT "Complete Genome Sequence of the Beer Spoilage Organism Pediococcus
RT claussenii ATCC BAA-344T.";
RL J. Bacteriol. 194:1271-1272(2012).
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DR EMBL; CP003137; AEV95891.1; -; Genomic_DNA.
DR RefSeq; WP_014216085.1; NC_016605.1.
DR AlphaFoldDB; G8PBA2; -.
DR STRING; 701521.PECL_1674; -.
DR KEGG; pce:PECL_1674; -.
DR PATRIC; fig|701521.8.peg.1575; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_1_1_9; -.
DR OMA; YQWRTVM; -.
DR Proteomes; UP000005444; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008788; F:alpha,alpha-phosphotrehalase activity; IEA:InterPro.
DR GO; GO:0005993; P:trehalose catabolic process; IEA:InterPro.
DR CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR InterPro; IPR012769; Trehalose_TreC.
DR NCBIfam; TIGR02403; trehalose_treC; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF217; TREHALOSE-6-PHOSPHATE HYDROLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AEV95891.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005444}.
FT DOMAIN 10..413
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 548 AA; 63703 MW; 6F627D2EBCA90B46 CRC64;
MSFKDKVIYQ IYPKSFYDSN NDGIGDLRGI IDKIPYIAKL NIDMIWFNPF FISPQYDNGY
DIADYYKIDP RFGTMADFEE LVAKLKEHKI GIMLDMVLNH TSTEHEWFKK ALAGDKHYQD
YYYIREPKPD GSLPTNWESK FGGNAWEPFG NTGKYYLHLY EKRQADLDWH NPEVRQELFK
VINFWRDKGV NGFRFDVINV TGKDEKLVDA PAGTESKYLY TDTPIVQKYL QEMNRASFGK
DSTSITVGEM SSTTIPNSIQ YTLESNHELS MVFTFHHLKV DYDHGEKWSK VPFDFKALKQ
TLNEWQVGMD EGNGWNALFW NNHDQPRAIN RFGDPVHYRN KSAEMLATTM HLLRGTPYIY
QGEEIGMSDP DYQSMDDYVD IEALNAYKML LEKGKSAEEA FEIIKSKARD NSRTPMQWDN
SVNAGFSQHT PWLKPTNQDE VNVENELANG EIFDYYQKLI SLRKGYPIIS EGSYEPFLMD
HPSVFGYLRR YNGQTLIVLN NFYGKSTTVA IPKELQQKAQ ILINNYPEDL VLSDNVELQP
YQSVAFLL
//